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pro vyhledávání: '"J.M. Sánchez-Montero"'
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Akademický článek
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Autor:
María J. Hernáiz, Jose‐Vicente Sinisterra, J.M. Sánchez-Montero, P. Domínguez de María, Carlos A. Garcia-Burgos, Andrés R. Alcántara, R.M. de la Casa, J.D. Carballeira
Publikováno v:
Current Organic Chemistry. 10:1053-1066
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c9adcf742ebdd3938f4b86f9ba61ca10
https://doi.org/10.2174/138527206777698057
https://doi.org/10.2174/138527206777698057
Publikováno v:
Enzyme and Microbial Technology. 38:599-609
Using fed-batch controlled fermenter conditions and oleic acid as the only carbon source, a new crude lipase from Candida rugosa ATCC 14830 (UAB) was produced. This lipase is a mixture of Lip2 (43%) and Lip3 (57%) and shows different composition in i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f4d3392f0492699a645290cc3d618d0d
https://doi.org/10.1016/j.enzmictec.2005.05.017
https://doi.org/10.1016/j.enzmictec.2005.05.017
Autor:
Steve W. Elson, Manuel Valmaseda, Maria-Soledad de Castro-Alvarez, Jose‐Vicente Sinisterra, Emilio Alvarez, J.M. Sánchez-Montero, Fernando Cardenas
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 14:111-123
A total of 969 microbial strains were isolated from soil samples and tested to determine their lipolytic activity by employing screening techniques on solid and in liquid media. Ten lipase-producing microorganisms were selected and their taxonomic id
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3728ac366e3a4c9974714610b553ff97
https://doi.org/10.1016/s1381-1177(00)00244-7
https://doi.org/10.1016/s1381-1177(00)00244-7
Autor:
Andrés R. Alcántara, Juan A. Hermoso, I. Borreguero, José V. Sinisterra, J.M. Sánchez-Montero, Angel Rumbero
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 11:1013-1024
The regioselective acylation of different phenylalkanediols catalysed by porcine pancreatic lipase (PPL) was used for modelling the enzymatic substrate recognition. Thus, different racemic or prochiral (1,n)-diols, with n ranging from 2 to 6, were re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::34de144ca03e3752be7761079d5f187a
https://doi.org/10.1016/s1381-1177(00)00086-2
https://doi.org/10.1016/s1381-1177(00)00086-2
Autor:
J.M. Sánchez-Montero, Fernando Cardenas, Steve W. Elson, M. S. De Castro-Alvarez, Jose‐Vicente Sinisterra, E. Alvarez
Publikováno v:
Biocatalysis and Biotransformation. 19:315-329
Three novel lipase-producing microorganisms have been isolated from 526 actinomycete strains by employing screening techniques on solid media. Time-course and scale-up of enzyme production were analyzed. The lipases, produced by microorganisms belong
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8424231cfde1e41b7976b4c5a0904826
https://doi.org/10.3109/10242420109003647
https://doi.org/10.3109/10242420109003647
Publikováno v:
Biotechnology Letters. 21:123-128
Replacing the lactose used in the commercial preparation of lipase from Candida rugosa by dextrans with different molecular weight, several preparations with enhanced activities in esterification of (R,S)-ibuprofen in organic medium were obtained. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0f87ba90437b3c34505ef004496b3093
https://doi.org/10.1023/a:1005426101080
https://doi.org/10.1023/a:1005426101080
Publikováno v:
Biotechnology Techniques. 12:823-827
Thermogravimetric and differential thermal analysis have shown that lyophilized Candida rugosa lipase A has more water bonded to it than isoenzyme lipase B: respectively 522 and 220 molecules of water per molecule of lipase. This may explain the diff
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fce54d304ea5da86d56ea4c0cf308019
https://doi.org/10.1023/a:1008896030387
https://doi.org/10.1023/a:1008896030387
Autor:
E. F. Llama, Ana Gradillas, C. Del Campo, J.M. Sánchez-Montero, M. Garcia, Jose‐Vicente Sinisterra
Publikováno v:
Biotechnology Letters. 19:999-1004
sThe hydrolysis of several esters catalyzed by lipase of Candida rugosa was used to analyse the interaction between the ester substrate and the active site and the geometry and steric restrictions of ‘alk‘, ‘ar‘ and ‘h‘ subsites. Using 4-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ae29e4e452f9bc2cb4a66e711e5d0980
https://doi.org/10.1023/a:1018447301016
https://doi.org/10.1023/a:1018447301016